1H NMR studies of the binding of bacteriophage-M13-encoded gene-5 protein to oligo(deoxyadenylic acid)s of varying length.
1H NMR studies of the binding of bacteriophage-M13-encoded gene-5 protein to oligo(deoxyadenylic acid)s of varying length.
复制标题
噬菌体 M13 编码的基因 5 蛋白与不同长度的寡聚(脱氧腺苷酸)结合的 1 H NMR 研究。
DOI:
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发表时间:
1982
期刊:
影响因子:
--
通讯作者:
C. W. Hilbers
中科院分区:
文献类型:
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作者:
N. Alma;B. Harmsen;J. V. van Boom;G. A. van der Marel;C. W. Hilbers
The binding of gene-5 protein to oligo(deoxyadenylic acid)s varying in length from 2 to 16 nucleotides has been studied by titrating the protein with the oligonucleotides and recording the 1H NMR spectra at 360 MHz. To obtain information about the mode of binding of the protein the aromatic parts of the spectra have been analysed by performing spectral simulations, starting from the assignments obtained from nuclear Overhausfer enhancements at 500 MHz [Alma, N. C. M., Harmsen, B. J. M., Hull, W. E., Van der Marel, G., Van Boom, J.H., and Hilbers, C. W. (1981) Biochemistry, 20, 4419-4428]. The 1H NMR spectra of the complexes of gene-5 protein with (dA)8, (dA)12 and (dA)16 appear to be identical except for differences in linewidth. The 1H NMR spectra of the complexes with the smaller oligonucleotides (dA)2, (dA)3 and (dA)4 differ from each other and from the spectra obtained from the complexes with longer oligonucleotides. However, binding of all oligonucleotides basically influences the same aromatic residues, namely two tyrosines and one phenylalanine. In the protein-oligonucleotide complexes, one protein monomer covers three nucleotide residues, in contrast to the stoichiometry of 1:4 found for protein-polynucleotide complexes. It was found that the binding to oligonucleotides is cooperative and ionic-strength-dependent but far less so than found for the binding to polynucleotides.
影响因子:
5.6
作者:
KOWALCZYKOWSKI, SC;LONBERG, N;VONHIPPEL, PH
通讯作者:
VONHIPPEL, PH
影响因子:
5.6
作者:
Torbet,J;Gray,DM;Gray,CW;Marvin,DA;Siegrist,H
通讯作者:
Siegrist,H